ID   A0A265QDW4_9FIRM        Unreviewed;       508 AA.
AC   A0A265QDW4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Agmatine deiminase {ECO:0000313|EMBL:OZV13927.1};
GN   ORFNames=CIW83_00355 {ECO:0000313|EMBL:OZV13927.1};
OS   Tissierella sp. P1.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC   Tissierella.
OX   NCBI_TaxID=1280483 {ECO:0000313|EMBL:OZV13927.1, ECO:0000313|Proteomes:UP000216906};
RN   [1] {ECO:0000313|EMBL:OZV13927.1, ECO:0000313|Proteomes:UP000216906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1 {ECO:0000313|EMBL:OZV13927.1,
RC   ECO:0000313|Proteomes:UP000216906};
RA   Bukhtiyarova P.A., Antsiferov D.V., Avakyan M.R., Frank Y.A., Ikkert O.P.,
RA   Pimenov N.V., Brasseur G., Tuovinen O.H., Karnachuk O.V.;
RT   "Isolation and Characterization of an Anaerobic Sulfidogenic Tissierella
RT   from Cu-bearing Coins.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZV13927.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NPMN01000001; OZV13927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A265QDW4; -.
DR   OrthoDB; 9814383at2; -.
DR   Proteomes; UP000216906; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09604; M1_APN_like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR034015; M1_LTA4H.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216906};
KW   Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT   DOMAIN          297..501
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   ACT_SITE        357
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   ACT_SITE        442
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT   BINDING         379
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ   SEQUENCE   508 AA;  58942 MW;  FD6BE32E601F6DA9 CRC64;
     MYWRSIMKKN KVLFIILLLI TILSLTSCKQ GKPLNADALI ARNINEINES KINEYRINVD
     LDTESMTYEG KQTVSYVNNT GIDLEDIYFH LYPNAFKSLA DAPILFNMEE KMSSLSYESG
     DMDIEKVIQN GKELEWSIGG DKDTILHIKL DKSLEKGKST ELYLEYKVKL PTTKDRFGYH
     DKGINFGNWY PILCVYDESG WNLDPYYKVG DPFYSEVSNY KVSITTPKDI IVASSGNIVS
     ENRKGDKKIY EIEGPLIRDF AWAASKDFII KEKKVEDTII KVYSITNDSN LINESLKIGE
     NSIKTFNKIF GKYPYGVYTI VNTEFPSGME YPGIVFISND YFHKHLISIL EKVIVHETAH
     QWWYGIVGNN QVKEPWLDEG LTTYSEVIYI NEVHGKKKAK EYYDQDIKLG YEYAVQYLGE
     NEVVNKPLSE FIGWDDYGLL VYTRAAMFVD RIKEDFGEET LYKILNKYYE EYKFKNARTE
     DFIKICEEVT NTSFNGLVKE YLNGNKNR
//